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Kinetic mechanism of Enterococcus faeciumd-aspartate ligase.
Biochimie. 2019 Mar;158:217-223. doi: 10.1016/j.biochi.2019.01.012. Epub 2019 Jan 22.
Biochimie. 2019.
PMID: 30682389
Discovery of the first inhibitors of bacterial enzyme D-aspartate ligase from Enterococcus faecium (Aslfm).
Škedelj V, Perdih A, Brvar M, Kroflič A, Dubbée V, Savage V, O'Neill AJ, Solmajer T, Bešter-Rogač M, Blanot D, Hugonnet JE, Magnet S, Arthur M, Mainardi JL, Stojan J, Zega A.
Škedelj V, et al.
Eur J Med Chem. 2013 Sep;67:208-20. doi: 10.1016/j.ejmech.2013.06.017. Epub 2013 Jun 28.
Eur J Med Chem. 2013.
PMID: 23867605
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6-Arylpyrido[2,3-d]pyrimidines as novel ATP-competitive inhibitors of bacterial D-alanine:D-alanine ligase.
Škedelj V, Arsovska E, Tomašić T, Kroflič A, Hodnik V, Hrast M, Bešter-Rogač M, Anderluh G, Gobec S, Bostock J, Chopra I, O'Neill AJ, Randall C, Zega A.
Škedelj V, et al.
PLoS One. 2012;7(8):e39922. doi: 10.1371/journal.pone.0039922. Epub 2012 Aug 2.
PLoS One. 2012.
PMID: 22876277
Free PMC article.
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Evaluation of the published kinase inhibitor set to identify multiple inhibitors of bacterial ATP-dependent mur ligases.
Hrast M, Rožman K, Ogris I, Škedelj V, Patin D, Sova M, Barreteau H, Gobec S, Grdadolnik SG, Zega A.
Hrast M, et al. Among authors: skedelj v.
J Enzyme Inhib Med Chem. 2019 Dec;34(1):1010-1017. doi: 10.1080/14756366.2019.1608981.
J Enzyme Inhib Med Chem. 2019.
PMID: 31072165
Free PMC article.
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ATP-binding site of bacterial enzymes as a target for antibacterial drug design.
Škedelj V, Tomašić T, Mašič LP, Zega A.
Škedelj V, et al.
J Med Chem. 2011 Feb 24;54(4):915-29. doi: 10.1021/jm101121s. Epub 2011 Jan 14.
J Med Chem. 2011.
PMID: 21235241
Review.
No abstract available.
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